Page 58 - Read Online
P. 58
Mezhyrova et al. Microbiome Res Rep 2023;2:28 https://dx.doi.org/10.20517/mrr.2023.28 Page 17 of 17
24. Schägger H, von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the
range from 1 to 100 kDa. Anal Biochem 1987;166:368-79. DOI PubMed
25. Morgner N, Barth H, Brutschy B. A new way to detect noncovalently bonded complexes of biomolecules from liquid micro-droplets
by laser mass spectrometry. Aust J Chem 2006;59:109. DOI
26. Peetz O, Hellwig N, Henrich E, et al. LILBID and nESI: different native mass spectrometry techniques as tools in structural biology. J
Am Soc Mass Spectrom 2019;30:181-91. DOI PubMed PMC
27. Morgner N, Robinson CV. Massign: an assignment strategy for maximizing information from the mass spectra of heterogeneous
protein assemblies. Anal Chem 2012;84:2939-48. DOI PubMed
28. Henrich E, Peetz O, Hein C, et al. Analyzing native membrane protein assembly in nanodiscs by combined non-covalent mass
spectrometry and synthetic biology. Elife 2017;6:e20954. DOI PubMed PMC
29. Höltje V, van Duin J. MS2 phage induced lysis of E. coli depends upon the activity of the bacterial autolysins. In: Nombela C, editor.
Microbial Cell Wall Synthesis and Autolysis. Elsevier Science; 1984. p. 195-199. Available from: https://books.google.de/books/
about/Microbial_Cell_Wall_Synthesis_and_Autoly.html?id=c96EAAAAIAAJ&redir_esc=y. [Last accessed on 18 Jul 2023]
30. Maratea D, Young K, Young R. Deletion and fusion analysis of the phage φX174 lysis gene E. Gene 1985;40:39-46. DOI PubMed
31. Buckley KJ, Hayashi M. Lytic activity localized to membrane-spanning region of ϕX174 E protein. Mol Gen Genet 1986;204:120-5.
DOI PubMed
32. Witte A, Schrot G, Schön P, Lubitz W. Proline 21, a residue within the α-helical domain of ΦX174 lysis protein E, is required for its
function in Escherichia coli. Mol Microbiol 1997;26:337-46. DOI PubMed
33. Schmidt BF, Berkhout B, Overbeek GP, van Strien A, van Duin J. Determination of the RNA secondary structure that regulates lysis
gene expression in bacteriophage MS2. J Mol Biol 1987;195:505-16. DOI PubMed
34. Licis N, van Duin J, Balklava Z, Berzins V. Long-range translational coupling in single-stranded RNA bacteriophages: an evolutionary
analysis. Nucleic Acids Res 1998;26:3242-6. DOI PubMed PMC
35. Singh RK, Jaishankar J, Muthamilarasan M, Shweta S, Dangi A, Prasad M. Genome-wide analysis of heat shock proteins in C4 model,
foxtail millet identifies potential candidates for crop improvement under abiotic stress. Sci Rep 2016;6:32641. DOI PubMed PMC
36. Höltje JV, Fiedler W, Rotering H, Walderich B, van Duin J. Lysis induction of Escherichia coli by the cloned lysis protein of the phage
MS2 depends on the presence of osmoregulatory membrane-derived oligosaccharides. J Biol Chem 1988;263:3539-41. DOI PubMed
37. Brogden KA. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 2005;3:238-50. DOI
PubMed
38. Fuertes G, Giménez D, Esteban-Martín S, Sánchez-Muñoz OL, Salgado J. A lipocentric view of peptide-induced pores. Eur Biophys J
2011;40:399-415. DOI PubMed PMC
39. Žerovnik E. Viroporins vs. other pore-forming proteins: what lessons can we take? Front Chem 2021;9:626059. DOI PubMed PMC
40. Krishnan R S, Satheesan R, Puthumadathil N, Kumar KS, Jayasree P, Mahendran KR. Autonomously assembled synthetic
transmembrane peptide pore. J Am Chem Soc 2019;141:2949-59. DOI
41. Chamakura KR, Edwards GB, Young R. Mutational analysis of the MS2 lysis protein L. Microbiology 2017;163:961-9. DOI PubMed
PMC

